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Presents a discussion board for dialogue of latest discoveries, ways, and concepts in molecular biology. includes contributions from leaders of their fields and considerable references.
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Hu, P. D. Gershon, A. E. Hodel, and E A. Quiocho. mRNA cap recognition: dominant role of enhanced stacking interactions between methylated bases and protein aromatic side chains. Proc. Natl. Acad. Sci. USA 96, 49-54 (1999). 87. A. E. Hodel, P. D. Gershon, and E A. Quiocho. Structural basis for sequence-nonspecific recognition of 5'-capped mRNA by a cap-modifying enzyme. Mol. Cell. 1,443-447 (1998). 88. J. Marcotrigiano, A. Gingras, N. Sonenberg, and S, K. Burley. Cocrystal structure of the messenger RNA 5' cap-binding protein (elF4E) bound to 7-methyl-GDP.
Mutational analysis of the Saccharomyces cerevisiaeABD1 gene: cap methyltransferase activity is essential for cell growth. Mol. Cell. Biol. 16, 475-480 (1996). 15. S. P. Wang and S. Shuman. Structure-function analysis of the mRNA cap methyltransferase of Saccharomyces cerevisiae. J. Biol. Chem. 272, 14683-14689 (1997). 16. N. Saha, B. Schwer, and S. Shuman. Characterization of human, Schizosaccharomyces pombe and Candida albicans mRNA cap methyltransferases and complete replacement of the yeast capping apparatus by mammalian enzymes.
34 STEWARTSHUMAN Niewmierzycka and Clarke (83) also discern other methyltransferase motifs, including motif II (FPCDIVST in Abdlp) and motif III (SLKIGGHFFG in Abdlp). Motifs II and III are present in the cellular cap methyltransferases (Fig. 9). Although several of the conserved side chains that define motifs II and III have been subjected to alanine substitution in Abdlp, none of the residues analyzed are essential for Abdlp function in vivo. Thus, motifs II and III are unlikely to contribute directly to catalysis by Abdlp.